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  • 1
    Electronic Resource
    Electronic Resource
    Isolation and structure of the endogenous agonist of opioid receptor-like ORL 1 receptor (1995)
    [s.l.] : Nature Publishing Group
    Nature 377 (1995), S. 532-535 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/377532a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and characterization of a novel protease from culture filtrates of a Streptomyces sp. (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 141 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A fibrinolytic protease has been isolated from Streptomyces sp. culture filtrate by successive chromatography on Mono S and Sephadex G50. The purified protease had a molecular mass of 33 kDa and had an isoelectric point of 6.7. It showed a sharp pH optimum at 7.8 with maximal protease activity between 35 °C and 50 °C. Its amino acid composition and aminoterminal sequence (17 residues) were determined. The protein exibited marked hydrolytic activity toward the substrates N-Succ-(Ala)2-Pro-Phe-pNA (Km= 0.77 mM, Vmax= 24.2 μmol mg−1 min−1) and N-Succ-(Ala)2-Pro-Leu-pNA (Km= 0.92 mM, Vmax= 7.7 μmol mg−1 min−1). It was totally inhibited by α1-antitrypsin, d-Phe-Pro-Arg-chloromethylketone and sodium dodecyl sulfate but was insensitive to EDTA, dithiothreitol, phenylmethylsulfonyl fluoride, soybean trypsin inhibitor, pepstatin or elastatinal. In this respect, this protease differed in its physico-chemical and biochemical properties from other extracellular proteases previously found in bacteria and fungi. The results suggest that it has properties of chymotrypsin-like serine-type proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08387.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Cloning and characterization of the eapB and eapC genes of Cryphonectria parasitica encoding two new acid proteinases, and disruption of eapC (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 97-105 
    Details
    ISSN: 1617-4623
    Keywords: Key words Cryphonectria parasitica ; Acid proteinase ; eapB/C genes ; Gene disruption ; Heterologous protein degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Two new proteinases secreted by Cryphonectria parasitica, namely EapB and EapC, have been purified. The corresponding structural genes were isolated by screening a cosmid library, and sequenced. Comparison of genomic and cDNA sequences revealed that the eapB and eapC genes contain three and two introns, respectively. The products of the eapB and eapC genes as deduced from the nucleotide sequences, are 268 and 269 residues long, respectively. N-terminal amino acid sequencing data indicates that EapC is synthesized as a zymogen, which yields a mature 206-amino acid enzyme after cleavage of the prepro sequence. Similarly, sequence alignment studies suggest that EapB is secreted as a 203-residue form which shares extensive similarities not only with EapC but also with two other acid fungal proteinases. However, they display distinct structural features; for example, no cysteine residue is found in EapC. The eapC gene was mutated using a two-step gene replacement strategy which allowed the specific introduction of several stop codons at the beginning of the eapC coding sequence in an endothiapepsin-deficient (EapA-) C. parasitica strain. Although the resulting strain did not secrete EapC, it still exhibited residual extracellular proteolytic activity, which could be due to EapB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02191829
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning and characterization of theeapB andeapC genes ofCryphonectria parasitica encoding two new acid proteinases, and disruption ofeapC (1996)
    Springer
    Molecular genetics and genomics 250 (1996), S. 97-105 
    Details
    ISSN: 1617-4623
    Keywords: Cryphonectria parasitica ; Acid proteinase ; eapB/C genes ; Gene disruption ; Heterologous protein degradation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new proteinases secreted byCryphonectria parasitica, namely EapB and EapC, have been purified. The corresponding structural genes were isolated by screening a cosmid library, and sequenced. Comparison of genomic and cDNA sequences revealed that theeapB andeapC genes contain three and two introns, respectively. The products of theeapB andeapC genes as deduced from the nucleotide sequences, are 268 and 269 residues long, respectively. N-terminal amino acid sequencing data indicates that EapC is synthesized as a zymogen, which yields a mature 206-amino acid enzyme after cleavage of the prepro sequence. Similarly, sequence alignment studies suggest that EapB is secreted as a 203-residue form which shares extensive similarities not only with EapC but also with two other acid fungal proteinases. However, they display distinct structural features; for example, no cysteine residue is found in EapC. TheeapC gene was mutated using a two-step gene replacement strategy which allowed the specific introduction of several stop codons at the beginning of theeapC coding sequence in an endothiapepsin-deficient (EapA+)C. parasitica strain. Although the resulting strain did not secrete EapC, it still exhibited residual extracellular proteolytic activity, which could be due to EapB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02191829
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Entry of diphtheria toxin linked to concanavalin A into primate and murine cells (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 122 (1985), S. 193-199 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Diphtheria toxin linked by a disulfide bridge to concanavalin A was highly toxic to HeLa S3 and Vero cells, as well as to murine L cells. The cells could be protected with α-methyl mannoside, indicating that the conjugate binds mainly through its concanavalin A moiety. Treatment of Vero cells with phospholipase C, TPA (12-O-tetradecanoylphorbol-13-acetate), and vanadate, which strongly reduce the ability of the cells to bind free diphtheria toxin, had little protective effect against the conjugate, whereas SITS (L-acetamido-4′-isothiocyano-stilbene-2,2′disulfonic acid), which inhibits diphtheria toxin binding, as well as the subsequent entry, protected Vero cells, but not L cells. Both types of cells are protected against the conjugate by NH4Cl and monensin, indicating that an acidified compartment is necessary for entry into the cytosol. Exposure of cells, bound with surface conjugate, to low pH induced entry of the toxin into Vero cells, but not into L Cells. Phospholipase C, TPA, and vanadate did not protect L cells against the conjugate. It is concluded that toxin in the conjugate enters L cells by a route which involves low pH, but which is not identical to that in Vero cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041220205
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Identification of proteins of the yeast protein map using genetically manipulated strains and peptide-mass fingerprinting (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1519-1533 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces ; yeast protein map ; protein identification ; mass spectrometry ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this study we used genetically manipulated strains in order to identify polypeptide spots of the protein map of Saccharomyces cerevisiae. Thirty-two novel polypeptide spots were identified using this strategy. They corresponded to the product of 23 different genes. We also explored the possibilities of using peptide-mass fingerprinting for the identification of proteins separated on our gels. According to this strategy, proteins contained in spots are digested with trypsin and the masses of generated peptides are determined by matrix-assisted laser desorption-ionization mass spectrometry (MALDI-MS). The peptide masses are then used to search a yeast protein database for proteins that match the experimental data. Application of this strategy to previously identified polypeptide spots gave evidence of the feasibility of this approach. We also report predictions on the identities of nine unknown spots using MALDI-MS.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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